Golgi-disturbing agents

Dinter, André; Berger, Eric G.

doi:10.1007/s004180050256

Cited by 353 publications

(346 citation statements)

References 88 publications

(102 reference statements)

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“…In the present study we wanted to determine whether inhibitors that affect vesicular components and the Golgi also affect correct NP transport. NOC inhibits microtubule polymerization which leads to trans-Golgi network fragmentation, whereas BFA disrupt the anterograde transport, and forms the trans-Golgi tubular network [9]. ZWEHD is an inhibitor of inflammatory caspases and inhibits Golgi fragmentation [13].…”

Section: Discussionmentioning

confidence: 99%

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

et al. 2016

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Influenza A virus (IFV) replicates its genome in the nucleus of infected cells and uses the cellular protein transport system for genome trafficking from the nucleus to the plasma membrane. However, many details of the mechanism of this process, and its relationship to subsequent cytoplasmic virus trafficking, have not been elucidated. We examined the effect of nuclear transport inhibitors Leptomycin B (LB), 5,6 dichloro-1-b-D-ribofuranosyl-benzimidazole (DRB), the vesicular transport inhibitor Brefeldin A (BFA), the caspase inhibitor ZWEHD, and microtubule inhibitor Nocodazole (NOC) on virus replication and intracellular trafficking of viral nucleoprotein (NP) from the nucleus to the ER and Golgi. Also, we carried out complementary studies to determine the effect of IFV on intracellular membranes. Inhibition of the CRM1 and TAP-P15 nuclear transport pathways by DRB and LB blocked completely the export of virus. Inhibition of vesicular trafficking by BFA, NOC, and ZWEHD also affected influenza infection. Interestingly, IFV infection induced fragmentation of the Golgi complex resulting in diffuse distribution of large and small vesicles throughout the cytoplasm. Live-cell microscopy revealed expansion of Golgi localization signals indicating progressive dispersion of Golgi positive structures, resulting in the disassembly of the Golgi ribbon structure. Other vesicular components (Rab1b, ARF1 and GBF1) were also found to be required for IFV infection. Furthermore, the exact step at which IFV infection disrupts vesicle trafficking was identified as the ER-Golgi intermediate compartment. These findings suggest that IFV NP is trafficked from the nucleus via the CRM1 and TAP pathways. IFV modulates vesicular trafficking inducing disruption of the Golgi complex. These studies provide insight on the ways in which IFV affects intracellular trafficking of different host proteins and will facilitate identification of useful pharmaceutical targets to abrogate virus replication.

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Section: Discussionmentioning

confidence: 99%

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

et al. 2016

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“…Bafilomycin A1, a blocker of vacuolar H + ‐ATPase, was used to identify the type of vesicles carrying the proteins 23. Brefeldin A inhibits the conventional endoplasmatic reticulum (ER)‐Golgi secretion pathway 24, 25.…”

Section: Resultsmentioning

confidence: 99%

Interaction of extracellular S100A4 with RAGE prompts prometastatic activation of A375 melanoma cells

Herwig

Belter

Wolf

et al. 2016

J Cellular Molecular Medi

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S100A4, a member of the S100 protein family of EF‐hand calcium‐binding proteins, is overexpressed in various tumour entities, including melanoma, and plays an important role in tumour progression. Several studies in epithelial and mesenchymal tumours revealed a correlation between extracellular S100A4 and metastasis. However, exact mechanisms how S100A4 stimulates metastasis in melanoma are still unknown. From a pilot experiment on baseline synthesis and secretion of S100A4 in human melanoma cell lines, which are in broad laboratory use, A375 wild‐type cells and, additionally, newly generated A375 cell lines stably transfected with human S100A4 (A375‐hS100A4) or human receptor for advanced glycation endproducts (A375‐hRAGE), were selected to investigate the influence of extracellular S100A4 on cell motility, adhesion, migration and invasion in more detail. We demonstrated that A375 cells actively secrete S100A4 in the extracellular space via an endoplasmic reticulum‐Golgi‐dependent pathway. S100A4 overexpression and secretion resulted in prometastatic activation of A375 cells. Moreover, we determined the influence of S100A4‐RAGE interaction and its blockade on A375, A375‐hS100A4, A375‐hRAGE cells, and showed that interaction of RAGE with extracellular S100A4 contributes to the observed activation of A375 cells. This investigation reveals additional molecular targets for therapeutic approaches aiming at blockade of ligand binding to RAGE or RAGE signalling to inhibit melanoma metastasis.

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“…Scale bar=25 urn window of organizer specification and patterning had minimal or no discernable effects in all three equal-cleaving species. In addition, although monensin and BFA act through distinct molecular or subcellular processes (Dinter and Berger 1998;Mayer 2003;Mollenhauer et al 1990), they had seemingly identical effects on development in P VII/gala, suggesting that the observed phenotypes are not the result of a chemical-specific toxicity. Monensin and BFA radialization results in a similar loss of animal-vegetal extension in the three equal-cleaving species, indicating that radialization is similarly achieved through the inhibition of specification .…”

Section: Discussionmentioning

confidence: 95%

“…Although the 3D organizer has been demonstrated in gastropod, polyplacophoran, and scaphopod classes, direct comparisons are problematic due to differences in the experimental techniques of different studies . To comparatively characterize 3D in a more standardized fashion, we used two general inhibitors of protein processing and secretion, monensin and BFA (Dinter and Berger 1998;Mayer 2003;Mollenhauer et al 1990), to test for the presence and function of 3D patterning in the equalcleaving gastropods, P vulgata and L. stagnalis, the equal-cleaving chiton , Mopalia muscosa, and the polarlobe-forming scaphopod, Anta/is enta/is. We then documented the resulting radialized development in each , focusing in particular on M. muscosa.…”

Section: Springermentioning

confidence: 99%

“…Treatment with BFA and monensin BFA and monensin are small organic molecules used as pharmacological tools to provide a rapid and reversible inhibition of protein processing and secretion in eukaryotes (Dinter and Berger 1998;Mayer 2003;Mollenhauer et al 1990). Monensin inhibits 3D specification at specific timepoints in gastropod development (Kuhtreiber et al 1988), and because the target and/or function of each 107 chemical is highly conserved, both can be used to test for organizer presence and function in developmentally uncharacterized species, where genomic and molecular genetic tools are lacking.…”

Section: Collection and Culturingmentioning

confidence: 99%

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Brefeldin A or monensin inhibits the 3D organizer in gastropod, polyplacophoran, and scaphopod molluscs

et al. 2006

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In molluscs, the 3D vegetal blastomere acts as a developmental signaling center, or organizer, and is required to establish bilateral symmetry in the embryo. 3D is similar to organizing centers in other metazoans, but detailed comparisons are difficult, in part because its organizing function is poorly understood. To elucidate 3D function in a standardized fashion, we used monensin and brefeldin A (BFA) to rapidly and reversibly interfere with protein processing and secretion, thereby inhibiting the signaling interactions that underlie its specification and patterning . In the gastropods , Patella vulgata and Lymnaea stagnalis , the polyplacophoran, Mopalia muscosa, and the scaphopod, Antalis entalis, treatments initiated before the organizerdependent onset of bilateral cleavage resulted in radialization of subsequent development. In radialized P vulgata, L.

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Golgi-disturbing agents

Cited by 353 publications

References 88 publications

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

Influenza infection modulates vesicular trafficking and induces Golgi complex disruption

Interaction of extracellular S100A4 with RAGE prompts prometastatic activation of A375 melanoma cells

Brefeldin A or monensin inhibits the 3D organizer in gastropod, polyplacophoran, and scaphopod molluscs

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